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- W1969081014 abstract "Blue dextran – Sepharose and Cibacron blue 3G-A interact with pyruvate kinase of Neurospora crassa. The enzyme is readily released from the substituted Sepharose column by elution with 0.17 M potassium phosphate buffer (pH 7.9), or 2 mM fructose 1,6-diphosphate (FDP), but not with either of the substrates, ADP and phosphoenolpyruvate (PEP), at 2 mM. Cibacron blue 3G-A is a noncompetitive inhibitor of pyruvate kinase with respect to both substrates. It appears to compete with the allosteric effector, FDP, for binding to the enzyme surface. A lack of elution of the enzyme from the immobilized blue dextran matrix by adenine nucleotides and the absence of a difference spectrum in the 650- to 700-nm range suggest that a dinucleotide-fold substructure is not implicated in the dye binding sites on pyruvate kinase. The interaction of Cibacron blue 3G-A and this enzyme can be followed fluorometrically; incremental addition of the dye to the enzyme solution results in a progressive decrease in the fluorescence of surface tryptophanyl residues. The quenching of fluorescence of exposed aromatic groups is subject to reversal following addition of FDP to the pyruvate kinase – Cibacron blue complex." @default.
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- W1969081014 date "1980-05-01" @default.
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- W1969081014 title "Studies of the structure–function relationships of Neurospora crassa pyruvate kinase: interaction with blue dextran – Sepharose and Cibacron blue 3G-A" @default.
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- W1969081014 doi "https://doi.org/10.1139/m80-107" @default.
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